Protein phosphatase-1 binding to Scd5p is important for regulation of actin organization and endocytosis in yeast

Ji Suk Chang, Kenneth Henry, Bianka L. Wolf, Maribel Geli, Sandra K. Lemmon

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30 Scopus citations

Abstract

SCD5, an essential gene, encodes a protein important for endocytosis and actin organization in yeast. Previous two-hybrid screens showed that Scd5p interacts with Glc7p, a yeast Ser/Thr-specific protein phosphatase-1 (PP1) that participates in a variety of cellular processes. PPI substrate specificity in vivo is regulated by association with different regulatory or targeting subunits, many of which have a consensus PPI -binding site ((V/I)XF, with a basic residue at the -1 or -2 position). Scd5p contains two of these potential PPI-binding motifs: KVDF (amino acids 240-243) and KKVRF (amino acids 272-276). Deletion analysis mapped the PPI-binding domain to a region of Scd5p containing these motifs. Therefore, the consequence of mutating these two potential PPI-binding sites was examined. Although mutation of KVDF had no effect, alteration of KKVRF dramatically reduced Scd5p interaction with Glc7p and resulted in temperature-sensitive growth. Furthermore, this mutation caused defects in fluid phase and receptor-mediated endocytosis and actin organization. Overexpression of GLC7 suppressed the temperature-sensitive growth of the KKVRF mutant and partially rescued the actin organization phenotype. These results provide evidence that Sed5p is a PPI targeting subunit for regulation of actin organization and endocytosis or that Scd5p is a PPI substrate, which regulates the function of Scd5p in these processes.

Original languageEnglish (US)
Pages (from-to)48002-48008
Number of pages7
JournalJournal of Biological Chemistry
Volume277
Issue number50
DOIs
StatePublished - Dec 13 2002

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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